| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | prn |
| Uniprot No | P14283 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 41-142aa |
| 氨基酸序列 | IVKTGERQHGIHIQGSDPGGVRTASGTTIKVSGRQAQGILLENPAAELQFRNGSVTSSGQLSDDGIRRFLGTVTVKAGKLVADHATLANVGDTWDDDGIALY |
| 预测分子量 | 17.6 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是3-4条关于PRNP重组蛋白的参考文献及其摘要概括：
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1. **标题**：*NMR structure of the mouse prion protein domain PrP(121-231)*
**作者**：Riek, R., Hornemann, S., Wider, G., Billeter, M., Glockshuber, R., & Wüthrich, K.
**摘要**：该研究通过核磁共振(NMR)技术解析了重组表达的仓鼠朊蛋白(PrP)C端结构域(121-231)的三维结构，揭示了其α螺旋和β折叠的分布特征，为理解PrP^C与PrP^Sc的构象差异提供了结构基础。
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2. **标题**：*Recombinant prion protein refolded into a native-like conformation retains antibody binding and structural features of the native form*
**作者**：Jackson, G.S., Hill, A.F., & Collinge, J.
**摘要**：本文报道了通过大肠杆菌重组表达的朊蛋白(PrP)经体外折叠后形成与天然PrP^C相似的结构，并通过抗体结合实验验证其正确构象。研究还发现重组PrP的铜离子结合能力与天然蛋白一致，支持其功能相关性。
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3. **标题**：*In vitro conversion of full-length mammalian prion protein produces amyloid-like fibrils with minimal β-sheet structure*
**作者**：Baskakov, I.V., Legname, G., Prusiner, S.B., & Cohen, F.E.
**摘要**：作者通过重组表达的全长朊蛋白(PrP)在体外模拟病理条件，成功诱导其形成淀粉样纤维。研究发现，这些纤维虽具有类似PrP^Sc的聚集特性，但其β片层结构含量较低，提示构象转变的复杂性。
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4. **标题**：*Monoclonal antibodies define a shared epitope on recombinant prion protein and native prions*
**作者**：Korth, C., Stierli, B., Streit, P., Moser, M., Schaller, O., & Fischer, R.
**摘要**：该研究利用重组表达的PrP制备单克隆抗体，发现某些抗体可同时识别重组PrP和天然PrP^Sc，表明二者存在共同的构象表位，为朊病毒检测和疾病机制研究提供了工具。
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以上文献涵盖了重组朊蛋白的结构解析、功能验证、体外病理转化及抗体开发方向，均为该领域的经典研究。
**Background of PRN Recombinant Proteins**
Pertactin (PRN), a key virulence factor of *Bordetella pertussis*, the causative agent of whooping cough, has been a focal point in vaccine research since the late 20th century. PRN is an outer membrane protein that facilitates bacterial adhesion to host respiratory epithelial cells, playing a critical role in infection. Its inclusion in acellular pertussis vaccines (aP) in the 1990s marked a shift from whole-cell vaccines (wP) due to improved safety profiles, though efficacy concerns later emerged.
Recombinant PRN proteins are produced via genetic engineering, where the *prn* gene is cloned into expression systems (e.g., *E. coli* or yeast) to enable large-scale, pure antigen production. This method overcomes challenges in isolating PRN from *B. pertussis* cultures, ensuring consistency for vaccines. Structurally, PRN contains immunogenic regions, notably the Arg-Gly-Asp (RGD) motif, which mediates host cell binding and elicits protective antibody responses.
However, recent decades have seen the emergence of PRN-deficient *B. pertussis* strains, particularly in countries using aP vaccines. This adaptation, potentially driven by vaccine-induced selective pressure, has raised concerns about long-term vaccine efficacy. Researchers now explore updated formulations, including engineered PRN variants or multi-antigen approaches, to address pathogen evolution.
Beyond pertussis vaccines, PRN recombinant proteins are studied for applications in diagnostics, therapeutics, and understanding bacterial pathogenesis. Their role in immune evasion mechanisms and host-pathogen interactions remains an active research area. Despite challenges, PRN continues to be a model antigen for studying recombinant protein applications in vaccinology and bacterial adaptation.
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